Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
although Lon is originally identified as an ATP-dependent protease with fused AAA+ (ATPases associated with diverse cellular activities) and protease domains, analyses have recently identified LonC as a class of Lon-like proteases with no intrinsic ATPase activity. In contrast to the canonical ATP-dependent Lon present in eukaryotic organelles and prokaryotes, LonC contains an AAA-like domain that lacks the conserved ATPase motifs
evolution
-
evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases, Escherichia coli utilizes five different AAA+ proteases: Lon, ClpXP, ClpAP, HslUV, and FtsH
evolution
-
homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins
evolution
the enzyme is a member of the ATP-dependent protease family
evolution
-
the enzyme is a member of the ATPase superfamily
evolution
human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP
evolution
human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP
evolution
human Lon (hLon) is a mitochondrial AAA+ protein (ATPases associated with diverse cellular activities) belonging to the LonA protease subfamily
evolution
Lon is a highly conserved member of the AAA+ (ATPases associated with diverse cellular activities) protease family
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane. In eukarya, two Lon proteases are present: a mitochondrial and a peroxisomal form, encoded by two different genes
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane. In eukarya, two Lon proteases are present: a mitochondrial and a peroxisomal form, encoded by two different genes
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane. In eukarya, two Lon proteases are present: a mitochondrial and a peroxisomal form, encoded by two different genes
evolution
LonA from Escherichia coli belongs to the superfamily of AAA+ proteins, family S16 of proteases. The presence of an extended variable N-terminal region preceding the AAA+ modules is a characteristic feature of LonA proteases distinguishing them from other AAA+ proteins
evolution
phylogenetic analysis reveals that Lon-like-Ms and its homologs are members of the Lon family. The ATP-dependent Lon (La) protease is the most highly conserved member of the energy-dependent protease present in the cytosol of prokaryotes and in the mitochondria and peroxisomes of eukaryotes. While the LonA group is found in eukaryotes and bacteria, the LonB subfamily proteins are only found in archaea. Two genes (Msm 1569 and Msm 1754) encoding Lon occur in the genome sequence, and the encoded proteins may play different roles. Msm 1569 encodes a canonical LonB protease (Lon-Ms). Msm 1754 (Lon-like-Ms) differs considerably from previously reported Lon proteases
evolution
-
structural comparison of AAA+ modules between LonA and LonB reveals that the AAA+ modules of Lon proteases are separated into two distinct clades depending on their structural features. The H2-insert clade is characterized by the presence of both the PS-1 insertion and the H2 insertion. In the H2-insert clade, no member has an additional insertion, like Ins1, between alpha4 and beta2 in the RFC-B AAA+ module. Therefore, it is not appropriate to classify the AAA+ module of TonLonB as the H2-insert clade. Alternatively, the AAA+ module of LonB belongs to a new clade, named H2 & Ins1 insert clade is proposed. The AAA+ module of LonB belongs to the H2 & Ins1 insert clade (HINS clade), while the AAA+ module of LonA is a member of the HCLR clade
evolution
the enzyme belongs to the protease family S16 and to the superfamily of AAA+ proteins
evolution
the enzyme belongs to the protease fasmily S16
evolution
-
the enzyme is a member of the ATP-dependent protease family
-
evolution
-
phylogenetic analysis reveals that Lon-like-Ms and its homologs are members of the Lon family. The ATP-dependent Lon (La) protease is the most highly conserved member of the energy-dependent protease present in the cytosol of prokaryotes and in the mitochondria and peroxisomes of eukaryotes. While the LonA group is found in eukaryotes and bacteria, the LonB subfamily proteins are only found in archaea. Two genes (Msm 1569 and Msm 1754) encoding Lon occur in the genome sequence, and the encoded proteins may play different roles. Msm 1569 encodes a canonical LonB protease (Lon-Ms). Msm 1754 (Lon-like-Ms) differs considerably from previously reported Lon proteases
-
evolution
-
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane. In eukarya, two Lon proteases are present: a mitochondrial and a peroxisomal form, encoded by two different genes
-
malfunction
-
Hvlon can be deleted from the chromosome only when a copy of the wild type gene is provided in trans suggesting that Lon is essential for survival in this archaeon. The contents of bacterioruberins and some polar lipids were increased in the lon mutants suggesting that Lon is linked to maintenance of membrane lipid balance which likely affects cell viability in this archaeon
malfunction
-
altered expression levels of the enzyme are linked to some severe diseases such as epilepsy, myopathy, or lateral sclerosis
malfunction
homozygous deletion of Lonp1 causes early embryonic lethality, whereas its haploinsufficiency protects against colorectal and skin tumors. LONP1 knockdown inhibits cellular proliferation and tumor and metastasis formation, phenotypes, overview. LONP1 is necessary for proliferation and metastasis of melanoma cells
malfunction
in a lon mutant, the steady-state levels and the stability of the GacA protein are significantly elevated at the end of exponential growth, the expression of the sRNAs RsmY and RsmZ and that of dependent physiological functions such as antibiotic production are significantly enhanced. In starved cells, the loss of Lon function prolonged the half-life of the GacA protein. The lon mutant has a higher biocontrol activity per viable cell, but this positive effect appears to be compromised by a reduced fitness of the mutant in the rhizosphere on cucumber. Biocontrol of Pythium ultimum on cucumber roots requires fewer lon mutant cells than wild-type cells. In starved cells, the loss of Lon function prolonges the half-life of the GacA protein. The lon mutant exhibits increased aprA expression and antibiotic activity
malfunction
-
lon mutants are supersusceptible to ciprofloxacin, and exhibit a defect in cell division and in virulence-related properties, such as swarming, twitching and biofilm formation, despite the fact that the Lon protease is not a traditional regulator. The lon mutant has a defect in cytotoxicity towards epithelial cells, is less virulent in an amoeba model as well as a mouse acute lung infection model, and is impacted on in vivo survival in a rat model of chronic infection. The lon mutation leads to a downregulation of Type III secretion genes. The Lon protease also influenced motility and biofilm formation in a mucin-rich environment, defective virulence in vivo. Phenotype detailed overview
malfunction
-
overexpression of the enzyme increases tumorigenesis, high levels of LONP1 are a poor prognosis marker in human colorectal cancer and melanoma, phenotypes, overview
malfunction
the stem nodules in the host legume Sesbania rostrata formed by the lon mutant show little or no nitrogen fixation activity. The reb genes are highly expressed in the lon mutant, high expression of reb genes in part causes aberrance in the Azorhizobium caulinodans-Sesbania rostrata symbiosis
malfunction
a Lon trapping variant, which is able to translocate substrates but unable to degrade them, is established and used for substrate determinations by mass spectrometry
malfunction
altered expression levels of the human mitochondrial Lon protease (hLon) are linked to serious diseases including myopathies, paraplegia, and cancer. The enzymatic activities and the 3D structure of a hLon mutant lacking the first 156 amino acids are severely disturbed
malfunction
-
deletion of Lon's ATPase domain abrogates interactions with DNA. Substitution of positively charged amino acids in this domain in full-length Lon with residues conferring a net negative charge disrupts binding of Lon to DNA. These changes also affect the degradation of nucleic acid binding protein substrates of Lon, intracellular localization of Lon, and cell morphology. The DNA-binding defect of Lon protease affects plasmid replication initiator protein TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex. The phenotype of the DNA binding-defective Lon mutants is similar to that observed for Lon-deficient strains
malfunction
downregulation leads to increased starvation-induced autophagy, and accumulation of PTEN-induced putative kinase-1 (PINK1), an essential regulator of mitophagy. Enzyme Lon is involved in genetic diseases and Lon protease plays a crucial role in the process of cell adaptation to a hypoxic environment, overview. Hypoxia leads to Lon upregulation in several cell types in humans, including monocytic acute myelogeneous leukaemia (THP-1), cardiomyocytes, embryonic kidney (293T) cells, rhabdomyosarcoma cells, renal cell carcinoma (RCC4) stably expressing Von Hippel-Lindau protein (VHL)
malfunction
enzyme knockout is embryonically lethal in mice. Lon+/- mouse model, in which the expression of Lon is halved, is characterized by a lower tendency to develop cancer and a higher resistance to carcinogenic compounds than wild type counterparts. Accordingly, growth of Lon-silenced cancer cells in xenograft model is significantly reduced if compared to control cells, while cells overexpressing Lon grow more rapidly. In vivo, Lon overexpression favours glycolysis, facilitates proliferation, and capability to migrate and form metastasis of melanoma cells in nude mice
malfunction
mutation of the lon gene leads to the overproduction of amylovoran, increased T3SS gene expression and the nonmotile phenotype. Erwinia amylovora depends on the type III secretion system (T3SS) and the exopolysaccharide (EPS) amylovoran to cause disease, and deletion of the lon gene in the csrA mutant only rescues amylovoran production, but not T3SS. RcsA/RcsB accumulation suppresses motility and flhD transcription in the lon mutant. Expression of the csrB sRNA is suppressed by RcsA/RcsB accumulation in the lon mutant
malfunction
removal of the HI(CC) domain results in a dexadcrease in the activity of the peptidase center of the Ec-Lon protease and a loss of the regulatory effect of the ATPase center on the peptidase one, which is defined by the nature of the bound nucleotide in the intact enxadzyme. Deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form
malfunction
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
malfunction
-
substitution of alanine for Lon serine 654 results in repression of T3SS gene expression in the Citrus host through robust degradation of HrpG and reduced bacterial virulence
malfunction
the deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested
malfunction
the Lon mutant variant V217A/Q220A (LonVQ) forms a dodecamer with increased stability compared to wild-type. Cells expressing only LonVQ are healthier than Lon-deficient strains during normal growth and perform similarly to wild-type Lon in a panel of in vivo bioassays except for degradation of small heat shock proteins. At 37°C, the enzyme-ddeficient DELTAlon strain grows significantly slower than the wild-type strain and never establishes a true exponential phase, but loss of Lon activity is not deleterious to viability
malfunction
-
the wild-type strain shows continuous linear growth for 60 days, whereas growth is impeded at 30 and 50 days for mitochondrial and peroxisomal isozyme-deficient mutants DELTAPLon and DELTAMLon mutants, respectively, suggesting that PLon is more important for longevity than MLon. Conidia production dramatically increases with the PLon deletion strain but not with the MLon deletion strain. Mutant DELTAPLon strains are more sensitive to multiple stressors than DELTAMLon
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
the stem nodules in the host legume Sesbania rostrata formed by the lon mutant show little or no nitrogen fixation activity. The reb genes are highly expressed in the lon mutant, high expression of reb genes in part causes aberrance in the Azorhizobium caulinodans-Sesbania rostrata symbiosis
-
malfunction
-
in a lon mutant, the steady-state levels and the stability of the GacA protein are significantly elevated at the end of exponential growth, the expression of the sRNAs RsmY and RsmZ and that of dependent physiological functions such as antibiotic production are significantly enhanced. In starved cells, the loss of Lon function prolonged the half-life of the GacA protein. The lon mutant has a higher biocontrol activity per viable cell, but this positive effect appears to be compromised by a reduced fitness of the mutant in the rhizosphere on cucumber. Biocontrol of Pythium ultimum on cucumber roots requires fewer lon mutant cells than wild-type cells. In starved cells, the loss of Lon function prolonges the half-life of the GacA protein. The lon mutant exhibits increased aprA expression and antibiotic activity
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
the wild-type strain shows continuous linear growth for 60 days, whereas growth is impeded at 30 and 50 days for mitochondrial and peroxisomal isozyme-deficient mutants DELTAPLon and DELTAMLon mutants, respectively, suggesting that PLon is more important for longevity than MLon. Conidia production dramatically increases with the PLon deletion strain but not with the MLon deletion strain. Mutant DELTAPLon strains are more sensitive to multiple stressors than DELTAMLon
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
mutation of the lon gene leads to the overproduction of amylovoran, increased T3SS gene expression and the nonmotile phenotype. Erwinia amylovora depends on the type III secretion system (T3SS) and the exopolysaccharide (EPS) amylovoran to cause disease, and deletion of the lon gene in the csrA mutant only rescues amylovoran production, but not T3SS. RcsA/RcsB accumulation suppresses motility and flhD transcription in the lon mutant. Expression of the csrB sRNA is suppressed by RcsA/RcsB accumulation in the lon mutant
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
malfunction
-
suboptimal LonB expression affects the content of membrane carotenoids and other lipids. Haloferax volcanii mutant cells deficient in Lon content are more sensitive to puromycin compared to wild-type cells. Deregulation of the cellular concentration of bacterioruberins and other lipids affects membrane stability contributing to the lethal phenotype of the lon knockout mutant
-
metabolism
-
mitochondrial calpain 10 is selectively degraded by Lon protease under basal conditions and is enhanced under and oxidizing conditions, while cytosolic calpain 10 is degraded by the proteasome
metabolism
-
plant mitochondrial protein carbonylation, an irreversible oxidative protein modification that inactivates the protein function, and role of the ATP-dependent proteases in defending mitochondria against accumulation of carbonylated proteins, overview. In plants, carbonylated proteins are found in virtually all cellular compartments - cytosol, chloroplasts, peroxisomes, nucleus, and mitochondria - and in the entire plant life cycle with especially high levels at certain stages of growth and development. Carbonylated breakdown products of mitochondrial proteins might act as secondary messengers in retrograde signaling from plant mitochondria to the nucleus. mitochondria depend on a series of pathways that continuously monitor and remove oxidatively damaged proteins
metabolism
-
the enzyme has a global impact on the physiology of the euryarchaeon Haloferax volcanii, affecting key cellular processes as well as organism-specific so far unknown functions which may be required for survival/adaptation under extreme conditions
metabolism
a connection between Lon and the GacS/GacACsr regulatory system might exist
metabolism
ATP-dependent Lon protease of Escherichia coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome
metabolism
functions of Lon protease in human mitochondria, overview. Lon expression highly correlates with expression of heat shock 60 kDa protein-1 (HSPD1), heat shock 10 kDa protein-1 (HSPE1), heat shock 70 kDa protein-9 (HSPA9), and caseinolytic mitochondrial matrix peptidase proteolytic subunit (CLPP), which are all involved in the mitochondrial unfolded protein response (UPRmt)
metabolism
-
the enzyme has a global impact on the physiology of the euryarchaeon Haloferax volcanii, affecting key cellular processes as well as organism-specific so far unknown functions which may be required for survival/adaptation under extreme conditions
-
metabolism
-
a connection between Lon and the GacS/GacACsr regulatory system might exist
-
metabolism
-
mitochondrial calpain 10 is selectively degraded by Lon protease under basal conditions and is enhanced under and oxidizing conditions, while cytosolic calpain 10 is degraded by the proteasome
-
physiological function
a lon2 disruption mutant is mildly resistant to the inhibitory effects of indole-3-butyric acid on root elongation, resistant to the stimulatory effects of indole-3-butyric acid on lateral root production and display succinate dependence during seedling growth. lon2 mutants display defects in removing the type 2 peroxisome targeting signal PTS2 from peroxisomal malate dehydrogenase and reduced accumulation of 3-ketoacyl-CoA thiolase, another PTS2-containing protein, both defects are not apparent upon germination but appear in 5 to 8 days old seedlings. In lon2 cotyledon cells, matrix proteins are localized to peroxisomes in 4 days old seedlings but mislocalized to the cytosol in 8 days old seedlings. A PTS2-green fluorescent protein reporter sorts to peroxisomes in lon2 root tip cells but is largely cytosolic in more mature root cells. LON2 is needed for sustained matrix protein import into peroxisomes
physiological function
-
absence of Lon protease blocks paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocks a parallel increase in cell lysate viscosity likely to reflect DNA size
physiological function
-
deletion of genes cpxR and lon results in mutants highly similar to wild-type. In comparison with the wild-type, 1.5- to 3.3fold increases of fimbrial products such as Agf, Fim, and Pef fimbria are observed in the single and double mutants. lon single and cpxR and lon double mutants morphologically appear elongated in shape and produce 2.0- and 3.2fold increases, respectively, of capsular polysaccharide, which is a major antigenic component. Approximately 104fold attenuation assessed by analysis of LD50 of BALB/c mouse is observed by deleting the lon/cpxR genes
physiological function
-
Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible
physiological function
Lon-1 may be important in host adaptation from the arthropod to a warm-blooded host. Recombinant Lon-1 shows properties of an ATP-dependent chaperone protease in vitro but does not complement an Escherichia coli Lon mutant
physiological function
Lon-2 is engaged in cellular homeostasis
physiological function
-
Pim1-mediated proteolysis is required for elimination of oxidatively damaged proteins in mitochondria. Pim1 plays a prevalent role in mitochondrial protein quality control
physiological function
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
-
the Lon protease is a stress-responsive protein that is induced by multiple stressors, including heat shock, serum starvation, and oxidative stress. Lon induction, by pretreatment with low-level stress, protects against oxidative protein damage, diminished mitochondrial function, and loss of cell proliferation induced by toxic levels of hydrogen peroxide. Blocking Lon induction with Lon siRNA also blocks this induced protection
physiological function
-
the Lon protease and the SecB and DnaJ/Hsp40 chaperones are involved in the quality control of presecretory proteins in Escherichia coli. Mutations in the lon gene alleviate the cold-sensitive phenotype of a secB mutant. In comparison to the respective single mutants, the double secB lon mutant strongly accumulates aggregates of SecB substrates at physiological temperatures, suggesting that the chaperone and the protease share substrates. The main substrates identified in secB lon aggregates, namely proOmpF and proOmpC, are highly sensitive to specific degradation by Lon. In contrast, both substrates are significantly protected from Lon degradation by SecB. The chaperone DnaJ by itself protects substrates better from Lon degradation than SecB or the complete DnaK/DnaJ/GrpE chaperone machinery
physiological function
-
transposon inactivation of ycgE, encoding a putative transcriptional regulator, leads to decreased multidrug susceptibility in an Escherichia coli lon mutant. The multidrug susceptibility phenotype e.g., to tetracycline and beta-lactam antibiotics, requires the inactivation of both lon and ycgE. In this mutant, a decreased amount of OmpF porin contributes to the lowered drug susceptibility, with a greater effect at 26°C than at 37°C
physiological function
lon disruption mutants show increased UV sensitivity, and produce higher levels of tabtoxin than the wild-type. Strains with lon disruption elicit the host defense system more rapidly and strongly than the wild-type strain, suggesting that the Lon protease is essential for systemic pathogenesis
physiological function
-
mitochondrial proteins aggregate to a substantial extent if they are challenged by either heat stress or reactive oxygen. As an important aspect of quality control, the proteolytic activity of Pim1 prevents the accumulation of these aggregation-prone polypeptides, resulting in prevention of proteotoxic effects
physiological function
purified Lon binds double stranded as well as single stranded DNA in the presence of elevated salt concentrations
physiological function
-
reduction of Lon to less than 10% of its normal level in Drosophila Schneider cells by RNAi knockdown results in increased abundance of mitochondrial transcription factor A, TFAM, and mitochondrial DNA copy number. In a corollary manner, overexpression of Lon reduces TFAM levels and mt DNA copy number. Induction of mitochondrial DNA depletion in Lon knockdown cells does not result in degradation of TFAM, thereby causing a dramatic increase in the TFAM:mitochondrial DNA ratio. The increased TFAM:mitochondrial DNA ratio in turn causes inhibition of mitochondrial transcription
physiological function
-
the enzyme controls membrane lipids composition and is essential for viability in the extremophilic haloarchaeon Haloferax volcanii
physiological function
-
AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. Ability of theLon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons, unfolding with robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin, overview
physiological function
ATP-dependent proteases, e.g. represented by Lon, are stress proteins that are induced in bacterial cells in response to unfavourable conditions. The enzyme negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway in Pseudomonas protegens, it is an important negative regulator of the Gac/Rsm signal transduction pathway in the organism. The Gac/Rsm signal transduction pathway controls secondary metabolism and suppression of fungal root pathogens via the expression of regulatory small RNAs, overview
physiological function
-
Lon is an ATPase associated with cellular activities protease that controls cell division in response to stress and also degrades misfolded and damaged proteins
physiological function
Lon protease is required to suppress the expression of the reb genes. Lon protease is also involved in the regulation of exopolysaccharide production and autoagglutination of bacterial cells
physiological function
-
protease Lon eliminates an immature or misfolded molybdoenzyme probably by targeting its inactive catalytic site, it is involved in the apoTorA degradation process
physiological function
-
the ATP-dependent Lon protease is a key component of the quality control system, which ensures the integrity and functionality of cellular proteins
physiological function
-
the enzyme can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation. Enzyme-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. Degron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation, degron binding regulates Lon ATPase and protease activity in addition to serving a recognition function. Inactivation of cell-division inhibitor SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
physiological function
the enzyme expression in reguated by HtrA2 serine protease, Lon1 protease is overexpressed in HtrA2-deficient cells, phenotype, overview. HtrA2 regulates mitochondrial proteins through its serine protease activity
physiological function
the enzyme expression in reguated by HtrA2 serine protease, Lon1 protease is overexpressed in HtrA2-deficient cells, phenotype, overview. HtrA2 regulates mitochondrial proteins through its serine protease activity
physiological function
-
the enzyme plays a key role in metabolic reprogramming by remodeling OXPHOS complexes and protecting against senescence. The protease is a central regulator of mitochondrial activity in oncogenesis. LONP1 is necessary for proliferation and metastasis of melanoma cells
physiological function
the enzyme plays a key role in metabolic reprogramming by remodeling OXPHOS complexes and protecting against senescence. The protease is a central regulator of mitochondrial activity in oncogenesis. Role of LONP1 in the regulation of mitochondrial function in cancer, overview
physiological function
-
the Lon protease is an ATP-dependent serine protease recognized as a key protease up-regulated under oxidative stress and involved in the removal of oxidized proteins, the mitochondrial inner membrane i-AAA protease is a crucial component of the defense against accumulation of carbonylated proteins. Due to the irreversible and unrepairable nature of protein carbonylation, proteolytic elimination of oxidatively damaged polypeptides is the major process of the mitochondrial protein quality control system under oxidative stress as first line of defense
physiological function
-
the Lon protease is essential for full virulence in Pseudomonas aeruginosa. The Lon protease is not a traditional regulator
physiological function
the Lon-insertion domain of LonC is involved both in Skplike chaperone activity and in recognition of unfolded protein substrates, structure of Lon-insertion domain is remarkably similar to the tentacle-like prong of the periplasmic chaperone Skp
physiological function
-
the main function of the enzyme is the control of protein quality and the maintenance of proteostasis by degradation of misfolded and damaged proteins, which occur in response to numerous stress conditions. It also participates in the regulation of levels of transcription factors that control pathogenesis, development and stress response
physiological function
-
a phosphorylation switch on Lon protease regulates bacterial type III secretion system in the host. Host-induced phosphorylation of the ATP-dependent protease Lon stabilizes HrpG, the master regulator of T3SS, conferring bacterial virulence. In rich medium, Lon represses the type III secretion system (T3SS) by degradation of HrpG via recognition of its N-terminus. Phosphorylation at Ser654 deactivates Lon proteolytic activity and attenuates HrpG proteolysis. Lon protease negatively regulates bacterial virulence by repressing hrc/hrp gene transcription. Phosphorylation of Lon is required for bacterial virulence and HR induction
physiological function
a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions, Lon affected proteins, overview. Fundamental functions of Lon in sulfur assimilation, nucleotide biosynthesis, amino acid and central energy metabolism, besides the superoxide stress response function. Lon protease affects the MetR regulon and function of proteins MetE and MetR
physiological function
in eukaryotes, Lon 1 is localized in the mitochondria and helps maintain proper cellular function. In humans, Lon is critical for maintaining the structure and integrity of mitochondria and has been found to selectively degrade accumulating proteins damaged by oxidative stress over their native counterparts
physiological function
Lon is a highly conserved cytosolic protease belonging to the AAA+ superfamily of ATPase, and acts as a major player in general protein quality control by degrading damaged or misfolded proteins. The proteolytic activity of Lon also contributes to the post-translational regulation of functional proteins. molecular mechanisms underlying Lon-mediated virulence regulation in Erwinia amylovora, an enterobacterial pathogen of apple. Gene lon expression is under the control of CsrA, possibly at both the transcriptional and post-transcriptional levels. CsrA might positively control both T3SS and amylovoran production partly by suppressing Lon. Lon negatively regulates amylovoran by targeting RcsA, but not RcsB. Lon-dependent degradation of RcsA regulates the expression of hrpS in Erwinia amylovora. Lon is essential for motility in Erwinia amylovora
physiological function
Lon is an essential, multitasking AAA+ protease regulating many cellular processes in species across all kingdoms of life. It plays crucial role in the maintenance of mitochondrial homeostasis. Structure-based regulation of Lon enzyme function, overview
physiological function
Lon protease (Lonp1) is a nuclear encoded, mitochondrial ATP-dependent serine peptidase, which mediates the selective degradation of mutant and abnormal proteins in the organelle, and helps in the maintenance of mitochondrial homeostasis. Chaperone-like functions of Lon are involved in the assembly of mitochondrial membrane complexes in yeast and in humans, and, at least in yeast, these functions are maintained after inactivation of proteolytic site and are prevented when ATP-binding site is mutated. Together with its proteolytic and chaperone activities, Lon ability to bind DNA is conserved from bacteria to mammalian mitochondria. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
physiological function
Lon protease (Lonp1) is a nuclear encoded, mitochondrial ATP-dependent serine peptidase, which mediates the selective degradation of mutant and abnormal proteins in the organelle, and helps in the maintenance of mitochondrial homeostasis. In humans, Lon is responsible for the degradation of: 1. stably folded proteins, including 5-aminolevulinic acid synthase, steroidogenic acute regulatory protein and mitochondrial transcription factor A (TFAM) and cytochrome c oxidase 4 isoform 1 (COX4-1), 2. misfolded and unfolded proteins, including glutaminase C, and 3. oxidatively-modified proteins, including mitochondrial aconitase and cystathionine beta-synthase. Lon proteolytic activity plays a role at different stages in the mitochondrial stress response. Chaperone-like functions of Lon are involved in the assembly of mitochondrial membrane complexes in yeast and in humans, and, at least in yeast, these functions are maintained after inactivation of proteolytic site and are prevented when ATP-binding site is mutated. Together with its proteolytic and chaperone activities, Lon ability to bind DNA is conserved from bacteria to mammalian mitochondria. Unlike bacterial Lon, human Lon binds specific ssDNA. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate. By selectively degrading TFAM and controlling TFAM/mtDNA ratio, Lon is responsible for mitochondrial transcription maintenance. Role of Lon protease in carcinogenesis, overview
physiological function
Lon protease (Lonp1) is a nuclear encoded, mitochondrial ATP-dependent serine peptidase, which mediates the selective degradation of mutant and abnormal proteins in the organelle, and helps in the maintenance of mitochondrial homeostasis. Together with its proteolytic and chaperone activities, Lon ability to bind DNA is conserved from bacteria to mammalian mitochondria. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
physiological function
Lon protease is one of the main participants of the proteome quality control (PQC) system supporting normal cell homeostasis. The PQC system involves molecular chaperones participating in the remodeling and disaggregation of cellular proteins and ATP-dependent peptide hydrolases, which control the level of regulatory proteins through selective proteolysis and eliminate potentially hazardous, anomalous, defective, and redundant proteins from cells through their exhaustive degradation. All proteases of the PQC system are bifunctional enzymes whose proteolytic activity is coupled with the simultaneous ATP hydrolysis and is characterized by a processive mechanism of the hydrolysis of protein targets (without the release of high-molecular-weight intermediates)
physiological function
-
Lon-DNA interactions are essential for Lon activity in cell division control. The ability of Lon to bind DNA is determined by its ATPase domain. This binding is required for processing protein substrates in nucleoprotein complexes, and Lon may help regulate DNA replication in response to growth conditions
physiological function
LonA from Escherichia coli plays a key role in the quality control system of the cell proteome. It destroys abnormal and defective polypeptides, as well as a number of regulatory proteins, according to a processive degradation mechanism
physiological function
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
physiological function
mitochondrial LON protease-dependent degradation of cytochrome c oxidase (CcO) subunits under hypoxia and myocardial ischemia. Lon is involved in the preferential turnover of phosphorylated CcO subunits under hypoxic/ischemic stress. Role of Lon in the degradation of phosphorylated subunits of CcO complex and importance of phosphorylation sites S40 of Vb and T52 of IVi1 subunits in Lon mediated degradation
physiological function
mitochondrial LON protease-dependent degradation of cytochrome c oxidase (CcO) subunits under hypoxia and myocardial ischemia. Lon is involved in the preferential turnover of phosphorylated CcO subunits under hypoxic/ischemic stress. Role of Lon in the degradation of phosphorylated subunits of CcO complex and importance of phosphorylation sites S40 of Vb and T52 of IVi1 subunits in Lon mediated degradation
physiological function
multidomain ATP-dependent Lon protease of Escherichia coli is one of the key enzymes of the quality control system of the cellular proteome. The HI(CC) domain of Ec-Lon protease is required for the formation of a functionally active enzyme structure and for the implementation of protein-protein interactions
physiological function
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
physiological function
-
the Lon AAA+ protease (LonA) is an evolutionarily conserved protease that couples the ATPase cycle into motion to drive substrate translocation and degradation
physiological function
the Lon AAA+ protease (LonA) plays important roles in protein homeostasis and regulation of diverse biological processes. Proposed Mg2+- and nucleotide-dependent assembly pathway of LonA, overview
physiological function
the mitochondrial Lon protease has been identified as an integral nucleoid core factor in human mitochondria, it is involved in selective protein turnover (including ribosomal proteins)12 and the ATP-dependent degradation of misfolded or damaged mitochondrial proteins. It also has a chaperone-like function in the assembly of certain mitochondrial complexes, which persists even if its proteolytic activity is impaired. Role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes. The mitochondrial Lon protease could be involved in the regulation of such fundamental processes as nucleoid packaging, mtDNA replication, mtDNA maintenance and recombination, and the assembly of mitochondrial ribosomes
physiological function
the mitochondrial Lon protease has been identified as an integral nucleoid core factor in human mitochondria, it is involved in selective protein turnover (including ribosomal proteins)12 and the ATP-dependent degradation of misfolded or damaged mitochondrial proteins. It also has a chaperone-like function in the assembly of certain mitochondrial complexes, which persists even if its proteolytic activity is impaired. Role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes. The mitochondrial Lon protease could be involved in the regulation of such fundamental processes as nucleoid packaging, mtDNA replication, mtDNA maintenance and recombination, and the assembly of mitochondrial ribosomes
physiological function
the protein quality control network (pQC) plays critical roles in maintaining protein and cellular homeostasis, especially during stress. Protease Lon is one of the central proteases responsible for protein quality control (pQC). It is the principal enzyme that degrades most unfolded or damaged proteins. Degradation by Lon also controls cellular levels of several key regulatory proteins. Analysis of biological roles of the Lon dodecamer. The enzyme dodecamer successfully completes many of the Lon protease's important regulatory functions while modifying substrate choice, perhaps to better manage protein quality control under conditions such as UV, heat, and oxidative stress
physiological function
together with its proteolytic and chaperone activities, Lon ability to bind DNA is conserved from bacteria to mammalian mitochondria. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
physiological function
together with its proteolytic and chaperone activities, Lon ability to bind mtDNA is conserved from bacteria to mammalian mitochondria. Escherichia coli Lon binds both single stranded DNA (ssDNA) and RNA (ssRNA), and double stranded DNA (dsDNA) in a non-specific manner, and this interaction enhances Lon ATPase and proteolytic activities. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
purified Lon binds double stranded as well as single stranded DNA in the presence of elevated salt concentrations
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
-
physiological function
-
Lon protease is required to suppress the expression of the reb genes. Lon protease is also involved in the regulation of exopolysaccharide production and autoagglutination of bacterial cells
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
ATP-dependent proteases, e.g. represented by Lon, are stress proteins that are induced in bacterial cells in response to unfavourable conditions. The enzyme negatively affects GacA protein stability and expression of the Gac/Rsm signal transduction pathway in Pseudomonas protegens, it is an important negative regulator of the Gac/Rsm signal transduction pathway in the organism. The Gac/Rsm signal transduction pathway controls secondary metabolism and suppression of fungal root pathogens via the expression of regulatory small RNAs, overview
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
lon disruption mutants show increased UV sensitivity, and produce higher levels of tabtoxin than the wild-type. Strains with lon disruption elicit the host defense system more rapidly and strongly than the wild-type strain, suggesting that the Lon protease is essential for systemic pathogenesis
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
Lon protease (Lonp1) is a nuclear encoded, mitochondrial ATP-dependent serine peptidase, which mediates the selective degradation of mutant and abnormal proteins in the organelle, and helps in the maintenance of mitochondrial homeostasis. Chaperone-like functions of Lon are involved in the assembly of mitochondrial membrane complexes in yeast and in humans, and, at least in yeast, these functions are maintained after inactivation of proteolytic site and are prevented when ATP-binding site is mutated. Together with its proteolytic and chaperone activities, Lon ability to bind DNA is conserved from bacteria to mammalian mitochondria. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
-
physiological function
-
the mitochondrial Lon protease has been identified as an integral nucleoid core factor in human mitochondria, it is involved in selective protein turnover (including ribosomal proteins)12 and the ATP-dependent degradation of misfolded or damaged mitochondrial proteins. It also has a chaperone-like function in the assembly of certain mitochondrial complexes, which persists even if its proteolytic activity is impaired. Role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes. The mitochondrial Lon protease could be involved in the regulation of such fundamental processes as nucleoid packaging, mtDNA replication, mtDNA maintenance and recombination, and the assembly of mitochondrial ribosomes
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
the enzyme can complement a LonB mutant in Haloferax volcanii suggesting functional conservation of LonB
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
Lon is a highly conserved cytosolic protease belonging to the AAA+ superfamily of ATPase, and acts as a major player in general protein quality control by degrading damaged or misfolded proteins. The proteolytic activity of Lon also contributes to the post-translational regulation of functional proteins. molecular mechanisms underlying Lon-mediated virulence regulation in Erwinia amylovora, an enterobacterial pathogen of apple. Gene lon expression is under the control of CsrA, possibly at both the transcriptional and post-transcriptional levels. CsrA might positively control both T3SS and amylovoran production partly by suppressing Lon. Lon negatively regulates amylovoran by targeting RcsA, but not RcsB. Lon-dependent degradation of RcsA regulates the expression of hrpS in Erwinia amylovora. Lon is essential for motility in Erwinia amylovora
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
physiological function
-
membrane-bound ATP-dependent Lon protease is essential for cell viability and quality control of proteins, it affects membrane carotenoid content in Haloferax volanii. Enzyme LonB controls carotenoid biosynthesis in Haloferax volcanii probably by degrading enzyme/s involved in this pathway. LonB is implicated in bacterioruberin biosynthesis and protein quality control
-
additional information
-
eukaryotic Lon possesses three domains, an N-terminal domain, an ATPase domain and a proteolytic domain
additional information
-
the AAA+ ATPase module and protease domain of Lon are part of a single polypeptide
additional information
the N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
additional information
-
the N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
additional information
-
the second alpha-helical domain plays a crucial role in ATP hydrolysis and enzyme binding to the target protein, while the first alpha-helical domain is not important for the manifestation of the catalytic properties of the enzyme, but it affects the functioning of Lon ATPase and peptidase sites and is involved in maintaining enzyme stability, participation of the first alpha-helical domain in the formation of three-dimensional structures of LonA proteases and/or their complexes with DNA
additional information
-
crystal structure determination of AAA+ module. Structural basis for the ATP-independent proteolytic activity of LonB proteases and reclassification of their AAA+ modules, overview. The isolated AAA+ module, having no bound nucleotide, adopts a conformation virtually identical to the ADP-bound conformation of AAA+ modules in the hexameric structure of TonLonB. Despite the conservation of functional motifs, the iAAA+ module has no ATPase activity. In the hexameric conformation, an arginine finger (Arg311) in one AAA+ module stabilizes negative charge of gamma-phosphate of ATP bound to the adjacent AAA+ module, which is essential for ATP hydrolysis
additional information
hLon's N-terminal domains are crucial for the overall structure of the hLon, maintaining a conformation allowing its proper functioning. Model on the quaternary structure of the full-length enzyme protein
additional information
-
hLon's N-terminal domains are crucial for the overall structure of the hLon, maintaining a conformation allowing its proper functioning. Model on the quaternary structure of the full-length enzyme protein
additional information
-
homology modeling of the Xanthomonas citri subsp. citri Lon P domain by using the Escherichia coli Lon structure as a template. Structural simulation using a phosphomimetic aspartic acid at position 654 of the P domain reveals the formation of two new H bonds between two structurally adjacent residues, A655 and S658 after phosphorylation of Ser654
additional information
Mg2+-activated LonA can operate as a diffusion-based chambered protease to degrade unstructured protein and peptide substrates efficiently in the absence of ATP. Mg2+-dependent remodeling of a substrate-binding loop and a potential metal-binding site near the Ser-Lys catalytic dyad, supported by biophysical binding assays and molecular dynamics simulations, domain arrangement and structural modeling, overview
additional information
the C-terminal part of the HI(CC) domain has an allosteric effect on the efficiency of the functioning of both ATPase and proteolytic sites of the enzyme, while the coiled-coil (CC) fragment of this domain interacts with the protein substrate. Analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for utodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
-
the C-terminal part of the HI(CC) domain has an allosteric effect on the efficiency of the functioning of both ATPase and proteolytic sites of the enzyme, while the coiled-coil (CC) fragment of this domain interacts with the protein substrate. Analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for utodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
the catalytic dyad required for peptide-bond hydrolysis is localized at Ser885-Lys896
additional information
the CC region is involved in the recognition of the nucleotide nature by the enzyme and the interaction of the enzyme with the protein substrate, effect of the coiled-coil (CC) region of the alpha-helical inserted domain of Escherichia coli Lon protease (Ec-Lon) on the functional activity of the enzyme, overview. The CC region is necessary for the formation and functioning of the ATPase and peptidase active centers, the occurrence of allosteric interactions between them, and for the implementation of proteolysis by a unique processive mechanism
additional information
the enzyme Ec-Lon is a bifunctional homohexameric enzyme, its subunit comprises an N-terminal noncatalytic region, two-domain ATPase module, and a proteolytic domain with serine-lysine endopeptidase activity
additional information
the enzyme has a Ser-Lys catalytic dyad
additional information
the enzyme's active site has a Ser-Lys catalytic dyad
additional information
-
the translational and rotational movements in the AAA+ module induced by the nucleotide have a profound impact on the Arg finger Arg484 location and P-loop conformation in ATPase sites. In the nucleotide-free state, the P loop is in an open conformation. In contrast, in the ADP-bound state, the P loop is well formed to accommodate the bound nucleotide
additional information
while proteolytic activity is restricted at the P domain, chaperone activity ismediated by the ATP-binding domain and the N-terminal domain. The chaperone and degradation chambers are contiguous and there is virtually no constriction of the chamber between the chaperone domain and the protease active sites
additional information
-
the enzyme has a Ser-Lys catalytic dyad
-
additional information
-
the enzyme has a Ser-Lys catalytic dyad
-
additional information
-
the enzyme has a Ser-Lys catalytic dyad
-
additional information
-
the enzyme has a Ser-Lys catalytic dyad
-